| SKRISOVSKA, Lenka, Cyril BOURGEOIS, Richard ŠTEFL, Sushma-Nagaraja GRELLSCHEID, Liliane KISTER, Philipp WENTER, David ELLIOTT, James STEVENIN a Frederic ALLAIN. The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction. EMBO REPORTS. Nature Publishing Group, London, UK: Nature Publishing Group, London, UK, 2007, roč. 8, č. 4, s. 372–379. ISSN 1469-221X. |
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@article{719419,
author = {Skrisovska, Lenka and Bourgeois, Cyril and Štefl, Richard and Grellscheid, SushmaandNagaraja and Kister, Liliane and Wenter, Philipp and Elliott, David and Stevenin, James and Allain, Frederic},
article_location = {Nature Publishing Group, London, UK},
article_number = {4},
keywords = {alternative splicing; NMR; protein-nucleic acid recognition; spermatogenesis; SELEX},
language = {eng},
issn = {1469-221X},
journal = {EMBO REPORTS},
title = {The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction},
volume = {8},
year = {2007}
}
TY - JOUR
ID - 719419
AU - Skrisovska, Lenka - Bourgeois, Cyril - Štefl, Richard - Grellscheid, Sushma-Nagaraja - Kister, Liliane - Wenter, Philipp - Elliott, David - Stevenin, James - Allain, Frederic
PY - 2007
TI - The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction
JF - EMBO REPORTS
VL - 8
IS - 4
SP - 372–379
EP - 372–379
PB - Nature Publishing Group, London, UK
SN - 1469221X
KW - alternative splicing
KW - NMR
KW - protein-nucleic acid recognition
KW - spermatogenesis
KW - SELEX
N2 - The RBMY (RNA binding motif gene on Y chromosome) protein encoded by the human Y chromosome is important for normal sperm development. Although its precise molecular RNA targets are unknown at present, it is suggested that human RBMY (hRBMY) participates in splicing in the testis. Using systematic evolution of ligands by exponential enrichment, we found that RNA stem loops capped by a C(A/U)CAA pentaloop are high affinity binding targets for hRBMY. Subsequent nuclear magnetic resonance structural determination of the hRBMY RNA recognition motif (RRM) in complex with a high affinity target showed two distinct modes of RNA recognition. First, the RRM beta sheet surface binds to the RNA loop in a sequence specific fashion. Second, the beta2 beta3 loop of the hRBMY inserts into the major groove of the RNA stem. The first binding mode might be conserved in the paralogous protein heterogeneous nuclear RNP G, whereas the second mode of binding is found only in hRBMY. This structural difference could be at the origin of the function of RBMY in spermatogenesis.
ER -
SKRISOVSKA, Lenka, Cyril BOURGEOIS, Richard ŠTEFL, Sushma-Nagaraja GRELLSCHEID, Liliane KISTER, Philipp WENTER, David ELLIOTT, James STEVENIN a Frederic ALLAIN. The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction. \textit{EMBO REPORTS}. Nature Publishing Group, London, UK: Nature Publishing Group, London, UK, 2007, roč.~8, č.~4, s.~372–379. ISSN~1469-221X.
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